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| Description | |
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| Catalogue Number | MAB3420-25UG |
| Brand Family | Chemicon® |
| Trade Name |
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| Description | Anti-Tau-1 Antibody, clone PC1C6 (mouse monoclonal) |
| Background Information | Tau, a microtubulebinding protein which serves to stabilize microtubules in growing axons, is found to be hyperphosphorylated in paired helical filaments (PHF), the major fibrous component of neurofibrillary lesions associated with Alzheimer’s disease. Hyperphosphorylation of Tau is thought to be the critical event leading to the assembly of PHF. Six Tau protein isoforms have been identified, all of which are phosphorylated by glycogen synthase kinase 3 (GSK 3). Cellular and subcellular localization: In situ, anti-tau-1 has a stringent specificity for the axons of neurons. The antibody does not stain the cell bodies or dendrites of neurons, nor does it stain any other cell type (4). However, this in vivo intracellular specificity is not maintained in culture: anti-tau-1 stains the axon, cell bodies, and dendrites of rat hippocampal neurons grown in culture (5). The specificity of anti-tau-1 was originally thought to represent the restricted expression of tau to axons. Later studies revealed that this specificity is dependant on the state of phosphorylation. In dephosphorylated samples (samples treated with alkaline phosphatase) anti-tau-1 stains astrocytes, perineuronal glial cells, and the axons, cell bodies and dendrites of neurons, while in untreated samples, anti-tau-1 stains only axons (6). (The epitope recognized by anti-tau-1 is probably at or near a phosphorylated site.) |
| Product Information | |
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| Format | Purified |
| Control |
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| Presentation | 0.02M phosphate buffer, pH 7.6, 0.25M NaCl, and 0.1% sodium azide |
| Quality Level | MQ100 |
| Applications | |
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| Application | Anti-Tau-1 Antibody, clone PC1C6 is an antibody against Tau-1 for use in IH & WB with more than 65 product citations. |
| Key Applications |
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| Application Notes | Western blot: Bovine brain microtubule proteins purified by two cycles of assembly and disassembly (9) are dissolved in SDS-PAGE sample buffer. Five micrograms of the microtuble preparation per lane is loaded onto a 4% to 20% SDS-PAGE gradient gel along side molecular weight markers (14.3 - 200 kD). After separation by electrophoresis, the proteins are blotted onto nitrocellulose. Tau is detected as a series of 5 bands (52-68 kD) with approximately 5 ng/mL of anti-tau-1. Immunohistochemistry: 5 μg/mL; stains axons in tissue primarily, however in culture Tau expression is not restricted to just axons. Optimal working dilutions must be determined by end user. Immunohistochemistry Protocol Dephosphorylation of tissue sections (optional) Dephosphorylation with alkaline phosphatase is recommended for staining neurofibrillary tangles in Alzheimers brain tissue with anti-tau-1 (6). This treatment changes the staining pattern of anti-tau-1 to include cell bodies, dendrites and axons of neurons. In untreated samples, anti-tau-1 stains axons only. 1. Incubate tissue sections at +32°C for 2.5 hours with constant agitation in the following solution: 100 mm Tris-HCl, pH 8.0; 130 units/mL alkaline phosphatase, 1 mm PMSF, 10 μg/mL pepstatin and 10 μg/mL leupeptin. 2. Rinse sections twice, 3 min per rinse, with 100 mm Tris-HCl, pH 8.0. Anti-tau-1 staining 1. Block non-specific binding by incubating sections in PBS containing 1% (v/v) normal animal serum, and 0.03% (w/v) Triton X-100. The animal serum should be from the same species as the secondary antibody. 2. Rinse 3 times with PBS, 3 min per rinse. 3. Incubate sections with anti-tau-1, approximately 5 μg/mL, diluted in PBS containing 1% (v/v) normal animal serum. 4. Wash with PBS, changing the solution 3 times over a 3 min period. 5. Detect with a standard secondary antibody detection system (10-13). |
| Biological Information | |
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| Immunogen | Purified denatured bovine microtubule associated proteins. |
| Clone | PC1C6 |
| Concentration | Please refer to lot specific datasheet. |
| Host | Mouse |
| Specificity | Binds to all known electrophoretic species of tau in human, rat and bovine brain (one-dimensional SDS-PAGE). However there is some unphosphorylated bias with clone PC1C6 as it seem to recognize only dephosphorylated serine sites at 195, 198, 199, and 202 {Szendrei, et Al 1993; http://www.ncbi.nlm.nih.gov/entrez/query.fcgi-cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7680727}. Also see Billingsley & Kincaid, 1997 Biochem J 323:577-591 for additional mapping information on PC1C6. |
| Isotype | IgG2a |
| Species Reactivity |
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| Antibody Type | Monoclonal Antibody |
| Entrez Gene Number |
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| Entrez Gene Summary | This gene encodes the microtubule-associated protein tau (MAPT) whose transcript undergoes complex, regulated alternative splicing, giving rise to several mRNA species. MAPT transcripts are differentially expressed in the nervous system, depending on stage of neuronal maturation and neuron type. MAPT gene mutations have been associated with several neurodegenerative disorders such as Alzheimers disease, Picks disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy. |
| Gene Symbol |
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| Purification Method | Protein A Purfied |
| UniProt Number |
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| UniProt Summary | FUNCTION: SwissProt: P10636 # Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N- terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. SIZE: 758 amino acids; 78878 Da SUBUNIT: Interacts with PSMC2 through SQSTM1 (By similarity). Interacts with SQSTM1 when polyubiquitinated. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components. TISSUE SPECIFICITY: Expressed in neurons. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.DEVELOPMENTAL STAGE: Four-repeat (type II) tau is expressed in an adult-specific manner and is not found in fetal brain, whereas three-repeat (type I) tau is found in both adult and fetal brain. DOMAIN: SwissProt: P10636 The tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats. PTM: Phosphorylation at serine and threonine residues in S-P or T- P motifs by proline-directed protein kinases (PDPK: CDC2, CDK5, GSK-3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in PHF-tau), and at serine residues in K- X-g-S motifs by MAP/microtubule affinity-regulating kinase (MARK) in Alzheimer diseased brains. Phosphorylation decreases with age. Phosphorylation within taus repeat domain or in flanking regions seems to reduce taus interaction with, respectively, microtubules or plasma membrane components. Phosphorylation on Ser-610, Ser- 622, Ser-641 and Ser-673 in several isoforms during mitosis. & Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity). PHF-tau can be modified by three different forms of polyubiquitination. Lys-48-linked polyubiquitination is the major form, Lys-6-linked and Lys-11-linked polyubiquitination also occur. & Glycation of PHF-tau, but not normal brain tau. Glycation is a non-enzymatic post-translational modification that involves a covalent linkage between a sugar and an amino group of a protein molecule forming ketoamine. Subsequent oxidation, fragmentation and/or cross-linking of ketoamine leads to the production of advanced glycation endproducts (AGES). Glycation may play a role in stabilizing PHF aggregation leading to tangle formation in AD. DISEASE: SwissProt: P10636 # In Alzheimer disease, the neuronal cytoskeleton in the brain is progressively disrupted and replaced by tangles of paired helical filaments (PHF) and straight filaments, mainly composed of hyperphosphorylated forms of TAU (PHF-TAU or AD P-TAU). & Defects in MAPT are a cause of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP17) [MIM:600274, 172700]; also called frontotemporal dementia (FTD) or historically termed Pick complex. This form of frontotemporal dementia is characterized by presenile dementia with behavioral changes, deterioration of cognitive capacities and loss of memory. In some cases, parkinsonian symptoms are prominent. Neuropathological changes include frontotemporal atrophy often associated with atrophy of the basal ganglia, substantia nigra, amygdala. In most cases, protein tau deposits are found in glial cells and/or neurons. & Defects in MAPT are a cause of pallido-ponto-nigral degeneration (PPND) [MIM:168610]. The clinical features include ocular motility abnormalities, dystonia and urinary incontinence, besides progressive parkinsonism and dementia. & Defects in MAPT are a cause of corticobasal degeneration (CBD). It is marked by extrapyramidal signs and apraxia and can be associated with memory loss. Neuropathologic features may overlap Alzheimer disease, progressive supranuclear palsy, and Parkinson disease. & Defects in MAPT are a cause of progressive supranuclear palsy (PSP) [MIM:601104, 260540]; also known as Steele-Richardson- Olszewski syndrome. PSP is characterized by akinetic-rigid syndrome, supranuclear gaze palsy, pyramidal tract dysfunction, pseudobulbar signs and cognitive capacities deterioration. Neurofibrillary tangles and gliosis but no amyloid plaques are found in diseased brains. Most cases appear to be sporadic, with a significant association with a common haplotype including the MAPT gene and the flanking regions. Familial cases show an autosomal dominant pattern of transmission with incomplete penetrance; genetic analysis of a few cases showed the occurrence of tau mutations, including a deletion of Asn-613. & Defects in MAPT may be a cause of hereditary dysphasic disinhibition dementia (HDDD) [MIM:607485]. HDDD is a frontotemporal dementia characterized by progressive cognitive deficits with memory loss and personality changes, severe dysphasic disturbances leading to mutism, and hyperphagia. SIMILARITY: Contains 4 Tau/MAP repeats. |
| Molecular Weight | 5 bands (52–68 kDa) |
| Product Usage Statements | |
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| Quality Assurance | Tested |
| Usage Statement |
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| Storage and Shipping Information | |
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| Storage Conditions | Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. |
| Packaging Information | |
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| Material Size | 25 μg |